Find research datasets worth reusing

opennotspecifiedNov 2020View details →

Fig. 1 in Detection of candidate proteins in the indican biosynthetic pathway of Persicaria tinctoria (Polygonum tinctorium) using protein-protein interactions and transcriptome analyses

Fig. 1. Chemical crosslinking assay in vitro and in vivo. Cytosolic (a) and microsomal (b) fractions and the protoplasts (c) were treated with chemical crosslinkers (BS3 and DSS, respectively). Treated samples were then subjected to SDS-PAGE using a 10% acrylamide gel for (a) and (b) and 7.5% for (c). Proteins that reacted against the anti-PtIGS antibody were detected by western blotting. "I" indicates PtIGS monomer. "II" denotes molecules larger than the monomer.

opennotspecifiedNov 2020View details →

Fig. 5 in Detection of candidate proteins in the indican biosynthetic pathway of Persicaria tinctoria (Polygonum tinctorium) using protein-protein interactions and transcriptome analyses

Fig. 5. The validation of the expression amount of candidates, which might relate to the indican biosynthesis pathway, by qRT-PCR. a, Indican synthase (PtIGS) and the degradation enzyme (PtBGL); b, indole synthesis-related proteins; c, proteins that might relate to the indole oxidation; d, UDP-glucose biosynthesis enzymes and transport proteins that might relate to the indican biosynthesis pathway. Each error bar shows the standard error. The detailed values of (a) and (b) are indicated in Supplementary Table 4S. Those values of (c) and (d) are showed in Tables 4 and 5, respectively.

Fig. 5 in L-DOPA synthesis in Mucuna pruriens (L.) DC. is regulated by polyphenol oxidase and not CYP 450/tyrosine hydroxylase: An analysis of metabolic pathway using biochemical and molecular markers

Fig. 5. The amplicons generated using degenerate primer approach. (a) Lane M-DNA ladder, Lane 1–250 bp amplicon generated using MTH –F and MTH-R primer pairs of TH gene (b) Lane M-DNA ladder, Lane 1 and 2–800 bp amplicon using primers deduced from the peptide sequence derived through LCMS/MS.

Fig. 4 in L-DOPA synthesis in Mucuna pruriens (L.) DC. is regulated by polyphenol oxidase and not CYP 450/tyrosine hydroxylase: An analysis of metabolic pathway using biochemical and molecular markers

Fig. 4. Effect of enzyme inhibitors on L-DOPA production in callus cultures of M. pruriens was estimated using HPTLC. The culture without inhibitor was treated as negative control and cultures with different concentration of the inhibitor were the test samples. (Control-untreated, C = Cimetidine at 1.98 μM and 19.8 μM; Q = Quinidine at 1.46 μM and 14.6 μM; A = L-ascorbic acid at 567 μM and 851 μM; K = Kojic acid at 703 μM and 1055 μM).

Fig. 3 in L-DOPA synthesis in Mucuna pruriens (L.) DC. is regulated by polyphenol oxidase and not CYP 450/tyrosine hydroxylase: An analysis of metabolic pathway using biochemical and molecular markers

Fig. 3. Effect of substrate concentration on partially purified enzymes. The assay was performed for PPO activity with 50 mM catechol as substrate at pH 6.0 while keeping the temperature for reaction at 30 ◦ C. For TH activity, 30 mM L-tyrosine was the substrate and assay done at pH 7.0 and 25 ◦ C.

Fig. 2 in L-DOPA synthesis in Mucuna pruriens (L.) DC. is regulated by polyphenol oxidase and not CYP 450/tyrosine hydroxylase: An analysis of metabolic pathway using biochemical and molecular markers

Fig. 2. Effect of pH on the activity of partially purified enzymes from Mucuna pruriens. The assay was performed using 50 mM catechol and 30 mM L-tyrosine as substrates for the PPO and TH enzyme activity, respectively. Four different buffers with their optimal buffering capacity in the pH range of 3–10 were used in separate assays.

Fig. 7 in L-DOPA synthesis in Mucuna pruriens (L.) DC. is regulated by polyphenol oxidase and not CYP 450/tyrosine hydroxylase: An analysis of metabolic pathway using biochemical and molecular markers

Fig. 7. Homology modelling and secondary structure prediction of PPO enzyme from Mucuna pruriens (a) Predicted secondary structure of PPO (b) Phyre2 protein model for PPO with 3D model dimensions (in Å) (X:49.941 Y:64.463 Z:57.979). Image colored by rainbow N → C terminus (c) Three dimensional SWISS protein model for PPO enzyme with two active copper binding ligands (copper ions bridging oxygen moiety is illustrated as small yellow spheres highlighted in the box), conserved histidine residues and metal complex interactions (in dotted lines). Chain A for Ligand 1: H.183, H.204, H.213, F.367, H.371; metal interactions: A:H.183, A:H.204, A:H.213. Chain A for Ligand 2: H.337, H.341, F.367, H.370, H.371; metal interactions: A:H.337, A:H.341, A:H.371). (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

Fig. 6. The 1800 in L-DOPA synthesis in Mucuna pruriens (L.) DC. is regulated by polyphenol oxidase and not CYP 450/tyrosine hydroxylase: An analysis of metabolic pathway using biochemical and molecular markers

Fig. 6. The 1800 bp amplicon of full-length PPO cDNA obtained after deducing the 5′and 3′ ends through RACE analysis. Lane 1- 1 Kb DNA marker, Lane 2 and 3 the amplicon in duplicate after amplification using gene specific primers.

opennotspecifiedDec 2020View details →

Fig. 3 in Lipoxygenase pathway in model bryophytes: 12-oxo-9(13),15-phytodienoic acid is a predominant oxylipin in Physcomitrella patens

Fig. 3. The proposed pathways of biosynthesis of major cyclopentenones in P. patens and M. polymorpha. β oxn, β oxidation.

opennotspecifiedDec 2020View details →

Fig. 2 in Lipoxygenase pathway in model bryophytes: 12-oxo-9(13),15-phytodienoic acid is a predominant oxylipin in Physcomitrella patens

Fig. 2. The electron impact mass spectra and fragmentation schemes (insets) for products 1 (A), 2 (B), and 3 (C).

opennotspecifiedDec 2020View details →

Fig. 1 in Lipoxygenase pathway in model bryophytes: 12-oxo-9(13),15-phytodienoic acid is a predominant oxylipin in Physcomitrella patens

Fig. 1. The GC-MS oxylipin profiles of P. patens (A, B) and M. polymorpha (C, D). A and C, the profiles of endogenous oxylipins (Me/TMSi), the mixed ion current chromatograms (m/z 149, 177, 210, 225, 238, 278, 306, 308, 311). B and D, profiles of oxylipins (Me/TMSi) biosynthesized upon the in vitro preincubations of P. patens and M. polymorpha with α linolenic acid. The experimental details are described under "Experimental".

Fig. 5 in Floro-pyrazolo[3,4-d]pyrimidine derivative as a novel plant activator induces two-pathway immune system

Fig. 5. The synthetic route of 1-methyl-4-substituted phenylamino pyrazolo [3,4-d] pyrimidine derivatives (P1).

Fig. 7 in Floro-pyrazolo[3,4-d]pyrimidine derivative as a novel plant activator induces two-pathway immune system

Fig. 7. The synthetic route of N-(1-methyl-1H-pyrazolo [3,4-d]pyrimidin-4-yl) substituted carboxamide derivatives (P3).

Fig. 6 in Floro-pyrazolo[3,4-d]pyrimidine derivative as a novel plant activator induces two-pathway immune system

Fig. 6. The synthetic route of 1-methyl-4-substituted ether pyrazolo [3,4-d] pyrimidine derivatives (P2).

Fig. 4 in Floro-pyrazolo[3,4-d]pyrimidine derivative as a novel plant activator induces two-pathway immune system

Fig. 4. Gene expression in Arabidopsis thaliana after treatment of chemicals. Bars (gray, PR1; black, PDF1.2) denote the mean ± STD of three independent biological replicates. (***P <0.01; **P <0.05; one-tailed t-test).

Fig. 3 in Comparison of carbohydrate partitioning and expression patterns of some genes involved in carbohydrate biosynthesis pathways in annual and biennial species of Cichorium spp.

Fig. 3. Relative gene expression of SUT1-3 in different tissues of chicory and endive at S1 and S2 stages. Transcript levels were determined by qPCR and normalized against the expression of the reference gene (RPL19). Transcript levels in different organs were expressed relative to the levels of leaves of chicory at S1. Values represent the mean of three biological replicates ± SE. Different letters indicate statistical significance P <0.05 (Duncan's multiple range test).

Fig. 7 in P450 variations bifurcate the early terpene indole alkaloid pathway in Catharanthus roseus and Camptotheca acuminata

Fig. 7. Molecular models of Catharanthus CYP72A1 and Camptotheca CYP72A564 and CYP72A565. (A) Backbone overlays of Catharanthus CYP72A1 and Camptotheca CYP72A564 and CYP72A565 models are shown with the alpha-carbon RMSD amongst CYP72A1, CYP72A564 and CYP72A565 depicted from green (0.0 Å) to yellow (3.0 Å) to red (4.5 Å). (B) SRS regions in CYP72A proteins shown with predicted substrate contact residues (gray fill). (C) Identical versus (D) different side chain residues predicted within 4.5 Å of loganin (aqua) docked in Catharanthus CYP72A1 (blue) and loganic acid (gray) docked in Camptotheca CYP72A564 (orange). (E) Identical versus (F) different side chain residues predicted within 4.5 Å of loganin (aqua) docked in Catharanthus CYP72A1 (blue) and loganic acid (gray) docked in Camptotheca CYP72A565 (rose).

Fig. 5 in P450 variations bifurcate the early terpene indole alkaloid pathway in Catharanthus roseus and Camptotheca acuminata

Fig. 5. Area of loganic acid, loganin and products from in vitro reconstitution assays conducted with full-length Camptotheca His6-tagged CPR1. Integrated areas from LC-MS analyses of purified His6-tagged CYP72A proteins reconstituted with full-length His6-tagged Caa CPR1 are shown for no NADPH (gray) and plus NADPH (gray slashed) reactions.

Fig. 2. CYP72A in P450 variations bifurcate the early terpene indole alkaloid pathway in Catharanthus roseus and Camptotheca acuminata

Fig. 2. CYP72A multiple sequence alignment. Signal anchor domain fusion of CYP72A565 into CYP72A564 is underlined; SRS regions are underlined in bold; predicted substrate contacts within 4.5 Å of loganic acid/loganin are gray-filled.

Fig. 1 in P450 variations bifurcate the early terpene indole alkaloid pathway in Catharanthus roseus and Camptotheca acuminata

Fig. 1. Proposed divergence of the TIA pathway between Camptotheca and Catharanthus. After 7-deoxyloganic acid hydroxylase (7DLH) converts 7-deoxyloganic acid to loganic acid, the pathways in these two species diverge. The Catharanthus pathway uses loganic acid methyltransferase (LAMT) to convert loganic acid into loganin and secologanin synthase (SLS) to convert loganin into secologanin. The Camptotheca pathway bypasses LAMT and uses secologanic acid synthase (SLAS) to metabolize loganic acid directly to secologanic acid.